Full text data of RAB2A
RAB2A
(RAB2)
[Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-2A
Ras-related protein Rab-2A
hRBCD
IPI00031169
IPI00031169 Ras-related protein Rab-2 (A or B) Ras-related protein Rab-2 (A or B) membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 1 cytoplasmic and membrane associated n/a found at its expected molecular weight found at molecular weight
IPI00031169 Ras-related protein Rab-2 (A or B) Ras-related protein Rab-2 (A or B) membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 1 cytoplasmic and membrane associated n/a found at its expected molecular weight found at molecular weight
UniProt
P61019
ID RAB2A_HUMAN Reviewed; 212 AA.
AC P61019; B2R5W8; B4DMQ5; P08886;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Ras-related protein Rab-2A;
GN Name=RAB2A; Synonyms=RAB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3057444; DOI=10.1093/nar/16.21.10368;
RA Tachibana K., Umezawa A., Kato S., Takano T.;
RT "Nucleotide sequence of a new YPT1-related human cDNA which belongs to
RT the ras gene superfamily.";
RL Nucleic Acids Res. 16:10368-10368(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2501306;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related
RT to yeast YPT1 and SEC4 products involved in secretion.";
RL J. Biol. Chem. 264:12394-12401(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ISOPRENYLATION AT CYS-211 AND CYS-212.
RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264;
RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R.,
RA Sinensky M., Balch W.E., Buss J.E., Der C.J.;
RT "Isoprenoid modification of rab proteins terminating in CC or CXC
RT motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
RN [10]
RP INTERACTION WITH PRKCI.
RX PubMed=14570876; DOI=10.1074/jbc.M309343200;
RA Tisdale E.J.;
RT "Rab2 interacts directly with atypical protein kinase C (aPKC)
RT iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-
RT phosphate dehydrogenase phosphorylation.";
RL J. Biol. Chem. 278:52524-52530(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-170 IN COMPLEX WITH GDP.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-
RT 5.";
RL Nature 436:415-419(2005).
CC -!- FUNCTION: Required for protein transport from the endoplasmic
CC reticulum to the Golgi complex.
CC -!- SUBUNIT: Interacts with PRKCI.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Lipid-anchor. Melanosome. Endoplasmic
CC reticulum membrane; Lipid-anchor (Potential). Golgi apparatus
CC membrane; Lipid-anchor (Potential). Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61019-2; Sequence=VSP_042917;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; X12953; CAA31411.1; -; mRNA.
DR EMBL; M28213; AAA60241.1; -; mRNA.
DR EMBL; AF498930; AAM21078.1; -; mRNA.
DR EMBL; BT019695; AAV38501.1; -; mRNA.
DR EMBL; AK297576; BAG59967.1; -; mRNA.
DR EMBL; AK312344; BAG35265.1; -; mRNA.
DR EMBL; AC068389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86827.1; -; Genomic_DNA.
DR EMBL; BC008929; AAH08929.1; -; mRNA.
DR PIR; B34323; B34323.
DR RefSeq; NP_001229573.1; NM_001242644.1.
DR RefSeq; NP_002856.1; NM_002865.2.
DR UniGene; Hs.369017; -.
DR PDB; 1Z0A; X-ray; 2.12 A; A/B/C/D=2-170.
DR PDBsum; 1Z0A; -.
DR ProteinModelPortal; P61019; -.
DR SMR; P61019; 2-170.
DR DIP; DIP-316N; -.
DR IntAct; P61019; 14.
DR MINT; MINT-5001132; -.
DR STRING; 9606.ENSP00000262646; -.
DR BindingDB; P61019; -.
DR PhosphoSite; P61019; -.
DR DMDM; 46577636; -.
DR PaxDb; P61019; -.
DR PRIDE; P61019; -.
DR DNASU; 5862; -.
DR Ensembl; ENST00000262646; ENSP00000262646; ENSG00000104388.
DR Ensembl; ENST00000531289; ENSP00000431846; ENSG00000104388.
DR GeneID; 5862; -.
DR KEGG; hsa:5862; -.
DR UCSC; uc003xud.2; human.
DR CTD; 5862; -.
DR GeneCards; GC08P061429; -.
DR HGNC; HGNC:9763; RAB2A.
DR HPA; CAB018781; -.
DR MIM; 179509; gene.
DR neXtProt; NX_P61019; -.
DR PharmGKB; PA162400618; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR KO; K07877; -.
DR OMA; HPTTNST; -.
DR OrthoDB; EOG7QK0CV; -.
DR PhylomeDB; P61019; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; RAB2A; human.
DR EvolutionaryTrace; P61019; -.
DR GeneWiki; RAB2A; -.
DR GenomeRNAi; 5862; -.
DR NextBio; 22766; -.
DR PRO; PR:P61019; -.
DR ArrayExpress; P61019; -.
DR Bgee; P61019; -.
DR CleanEx; HS_RAB2A; -.
DR Genevestigator; P61019; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 212 Ras-related protein Rab-2A.
FT /FTId=PRO_0000121066.
FT NP_BIND 13 21 GTP.
FT NP_BIND 61 65 GTP (By similarity).
FT NP_BIND 119 122 GTP.
FT NP_BIND 149 151 GTP.
FT REGION 2 19 Required for interaction with PRKCI.
FT MOTIF 35 43 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT LIPID 211 211 S-geranylgeranyl cysteine.
FT LIPID 212 212 S-geranylgeranyl cysteine.
FT VAR_SEQ 16 39 Missing (in isoform 2).
FT /FTId=VSP_042917.
FT CONFLICT 144 144 I -> M (in Ref. 2; AAA60241).
FT STRAND 4 14
FT HELIX 19 28
FT STRAND 43 50
FT STRAND 53 61
FT TURN 66 69
FT HELIX 73 76
FT STRAND 79 87
FT HELIX 91 95
FT HELIX 97 107
FT STRAND 113 119
FT HELIX 124 126
FT HELIX 131 141
FT STRAND 144 148
FT TURN 150 152
FT HELIX 156 169
SQ SEQUENCE 212 AA; 23546 MW; F8731E3F8FB399A3 CRC64;
MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK
SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN
EANGIKIGPQ HAATNATHAG NQGGQQAGGG CC
//
ID RAB2A_HUMAN Reviewed; 212 AA.
AC P61019; B2R5W8; B4DMQ5; P08886;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Ras-related protein Rab-2A;
GN Name=RAB2A; Synonyms=RAB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3057444; DOI=10.1093/nar/16.21.10368;
RA Tachibana K., Umezawa A., Kato S., Takano T.;
RT "Nucleotide sequence of a new YPT1-related human cDNA which belongs to
RT the ras gene superfamily.";
RL Nucleic Acids Res. 16:10368-10368(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2501306;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related
RT to yeast YPT1 and SEC4 products involved in secretion.";
RL J. Biol. Chem. 264:12394-12401(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ISOPRENYLATION AT CYS-211 AND CYS-212.
RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264;
RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R.,
RA Sinensky M., Balch W.E., Buss J.E., Der C.J.;
RT "Isoprenoid modification of rab proteins terminating in CC or CXC
RT motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
RN [10]
RP INTERACTION WITH PRKCI.
RX PubMed=14570876; DOI=10.1074/jbc.M309343200;
RA Tisdale E.J.;
RT "Rab2 interacts directly with atypical protein kinase C (aPKC)
RT iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-
RT phosphate dehydrogenase phosphorylation.";
RL J. Biol. Chem. 278:52524-52530(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-170 IN COMPLEX WITH GDP.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-
RT 5.";
RL Nature 436:415-419(2005).
CC -!- FUNCTION: Required for protein transport from the endoplasmic
CC reticulum to the Golgi complex.
CC -!- SUBUNIT: Interacts with PRKCI.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Lipid-anchor. Melanosome. Endoplasmic
CC reticulum membrane; Lipid-anchor (Potential). Golgi apparatus
CC membrane; Lipid-anchor (Potential). Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61019-2; Sequence=VSP_042917;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; X12953; CAA31411.1; -; mRNA.
DR EMBL; M28213; AAA60241.1; -; mRNA.
DR EMBL; AF498930; AAM21078.1; -; mRNA.
DR EMBL; BT019695; AAV38501.1; -; mRNA.
DR EMBL; AK297576; BAG59967.1; -; mRNA.
DR EMBL; AK312344; BAG35265.1; -; mRNA.
DR EMBL; AC068389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86827.1; -; Genomic_DNA.
DR EMBL; BC008929; AAH08929.1; -; mRNA.
DR PIR; B34323; B34323.
DR RefSeq; NP_001229573.1; NM_001242644.1.
DR RefSeq; NP_002856.1; NM_002865.2.
DR UniGene; Hs.369017; -.
DR PDB; 1Z0A; X-ray; 2.12 A; A/B/C/D=2-170.
DR PDBsum; 1Z0A; -.
DR ProteinModelPortal; P61019; -.
DR SMR; P61019; 2-170.
DR DIP; DIP-316N; -.
DR IntAct; P61019; 14.
DR MINT; MINT-5001132; -.
DR STRING; 9606.ENSP00000262646; -.
DR BindingDB; P61019; -.
DR PhosphoSite; P61019; -.
DR DMDM; 46577636; -.
DR PaxDb; P61019; -.
DR PRIDE; P61019; -.
DR DNASU; 5862; -.
DR Ensembl; ENST00000262646; ENSP00000262646; ENSG00000104388.
DR Ensembl; ENST00000531289; ENSP00000431846; ENSG00000104388.
DR GeneID; 5862; -.
DR KEGG; hsa:5862; -.
DR UCSC; uc003xud.2; human.
DR CTD; 5862; -.
DR GeneCards; GC08P061429; -.
DR HGNC; HGNC:9763; RAB2A.
DR HPA; CAB018781; -.
DR MIM; 179509; gene.
DR neXtProt; NX_P61019; -.
DR PharmGKB; PA162400618; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR KO; K07877; -.
DR OMA; HPTTNST; -.
DR OrthoDB; EOG7QK0CV; -.
DR PhylomeDB; P61019; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; RAB2A; human.
DR EvolutionaryTrace; P61019; -.
DR GeneWiki; RAB2A; -.
DR GenomeRNAi; 5862; -.
DR NextBio; 22766; -.
DR PRO; PR:P61019; -.
DR ArrayExpress; P61019; -.
DR Bgee; P61019; -.
DR CleanEx; HS_RAB2A; -.
DR Genevestigator; P61019; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 212 Ras-related protein Rab-2A.
FT /FTId=PRO_0000121066.
FT NP_BIND 13 21 GTP.
FT NP_BIND 61 65 GTP (By similarity).
FT NP_BIND 119 122 GTP.
FT NP_BIND 149 151 GTP.
FT REGION 2 19 Required for interaction with PRKCI.
FT MOTIF 35 43 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT LIPID 211 211 S-geranylgeranyl cysteine.
FT LIPID 212 212 S-geranylgeranyl cysteine.
FT VAR_SEQ 16 39 Missing (in isoform 2).
FT /FTId=VSP_042917.
FT CONFLICT 144 144 I -> M (in Ref. 2; AAA60241).
FT STRAND 4 14
FT HELIX 19 28
FT STRAND 43 50
FT STRAND 53 61
FT TURN 66 69
FT HELIX 73 76
FT STRAND 79 87
FT HELIX 91 95
FT HELIX 97 107
FT STRAND 113 119
FT HELIX 124 126
FT HELIX 131 141
FT STRAND 144 148
FT TURN 150 152
FT HELIX 156 169
SQ SEQUENCE 212 AA; 23546 MW; F8731E3F8FB399A3 CRC64;
MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK
SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN
EANGIKIGPQ HAATNATHAG NQGGQQAGGG CC
//
MIM
179509
*RECORD*
*FIELD* NO
179509
*FIELD* TI
*179509 RAS-ASSOCIATED PROTEIN RAB2; RAB2
;;RAB2A
*FIELD* TX
DESCRIPTION
Members of the Rab protein family are nontransforming monomeric
read moreGTP-binding proteins of the Ras superfamily that contain 4 highly
conserved regions involved in GTP binding and hydrolysis. Rabs are
prenylated, membrane-bound proteins involved in vesicular fusion and
trafficking. The mammalian RAB proteins show striking similarities to
the S. cerevisiae YPT1 and SEC4 proteins, Ras-related GTP-binding
proteins involved in the regulation of secretion.
CLONING
Zahraoui et al. (1989) isolated cDNAs encoding RAB2 and several other
human RAB proteins. See RAB5A (179512). The predicted 212-amino acid
human RAB2 protein shares 98% identity with rat Rab2. Northern blot
analysis revealed that the RAB2 gene was expressed as 1.1-, 2.5-, and
3.6-kb mRNAs in a human fibroblast cell line.
GENE FUNCTION
Tisdale and Balch (1996) stated that the RAB2 protein is a resident of
pre-Golgi intermediates and is required for protein transport from the
endoplasmic reticulum to the Golgi complex. They found that RAB2 is
essential for the maturation of pre-Golgi intermediates.
MAPPING
By analysis of the human genome database, Ni et al. (2002) mapped the
RAB2A gene to chromosome 8q12.1 and the RAB2B gene (607466) to
14q11.1-q11.2.
*FIELD* RF
1. Ni, X.; Ma, Y.; Cheng, H.; Jiang, M.; Guo, L.; Ji, C.; Gu, S.;
Cao, Y.; Xie, Y.; Mao, Y.: Molecular cloning and characterization
of a novel human Rab (Rab2B) gene. J. Hum. Genet. 47: 548-551, 2002.
2. Tisdale, E. J.; Balch, W. E.: Rab2 is essential for the maturation
of pre-Golgi intermediates. J. Biol. Chem. 271: 29372-29379, 1996.
3. Zahraoui, A.; Touchot, N.; Chardin, P.; Tavitian, A.: The human
rab genes encode a family of GTP-binding proteins related to yeast
YPT1 and SEC4 products involved in secretion. J. Biol. Chem. 264:
12394-12401, 1989.
*FIELD* CN
Victor A. McKusick - updated: 1/7/2003
Rebekah S. Rasooly - updated: 3/8/1999
*FIELD* CD
Victor A. McKusick: 7/9/1990
*FIELD* ED
carol: 01/15/2003
cwells: 1/9/2003
tkritzer: 1/7/2003
mgross: 3/10/1999
mgross: 3/9/1999
mgross: 3/8/1999
supermim: 3/16/1992
carol: 7/9/1990
*RECORD*
*FIELD* NO
179509
*FIELD* TI
*179509 RAS-ASSOCIATED PROTEIN RAB2; RAB2
;;RAB2A
*FIELD* TX
DESCRIPTION
Members of the Rab protein family are nontransforming monomeric
read moreGTP-binding proteins of the Ras superfamily that contain 4 highly
conserved regions involved in GTP binding and hydrolysis. Rabs are
prenylated, membrane-bound proteins involved in vesicular fusion and
trafficking. The mammalian RAB proteins show striking similarities to
the S. cerevisiae YPT1 and SEC4 proteins, Ras-related GTP-binding
proteins involved in the regulation of secretion.
CLONING
Zahraoui et al. (1989) isolated cDNAs encoding RAB2 and several other
human RAB proteins. See RAB5A (179512). The predicted 212-amino acid
human RAB2 protein shares 98% identity with rat Rab2. Northern blot
analysis revealed that the RAB2 gene was expressed as 1.1-, 2.5-, and
3.6-kb mRNAs in a human fibroblast cell line.
GENE FUNCTION
Tisdale and Balch (1996) stated that the RAB2 protein is a resident of
pre-Golgi intermediates and is required for protein transport from the
endoplasmic reticulum to the Golgi complex. They found that RAB2 is
essential for the maturation of pre-Golgi intermediates.
MAPPING
By analysis of the human genome database, Ni et al. (2002) mapped the
RAB2A gene to chromosome 8q12.1 and the RAB2B gene (607466) to
14q11.1-q11.2.
*FIELD* RF
1. Ni, X.; Ma, Y.; Cheng, H.; Jiang, M.; Guo, L.; Ji, C.; Gu, S.;
Cao, Y.; Xie, Y.; Mao, Y.: Molecular cloning and characterization
of a novel human Rab (Rab2B) gene. J. Hum. Genet. 47: 548-551, 2002.
2. Tisdale, E. J.; Balch, W. E.: Rab2 is essential for the maturation
of pre-Golgi intermediates. J. Biol. Chem. 271: 29372-29379, 1996.
3. Zahraoui, A.; Touchot, N.; Chardin, P.; Tavitian, A.: The human
rab genes encode a family of GTP-binding proteins related to yeast
YPT1 and SEC4 products involved in secretion. J. Biol. Chem. 264:
12394-12401, 1989.
*FIELD* CN
Victor A. McKusick - updated: 1/7/2003
Rebekah S. Rasooly - updated: 3/8/1999
*FIELD* CD
Victor A. McKusick: 7/9/1990
*FIELD* ED
carol: 01/15/2003
cwells: 1/9/2003
tkritzer: 1/7/2003
mgross: 3/10/1999
mgross: 3/9/1999
mgross: 3/8/1999
supermim: 3/16/1992
carol: 7/9/1990